UniProt ID | STE3_YEAST | |
---|---|---|
UniProt AC | P06783 | |
Protein Name | Pheromone a factor receptor | |
Gene Name | STE3 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 470 | |
Subcellular Localization |
Membrane Multi-pass membrane protein. |
|
Protein Description | Receptor for the peptide pheromone a factor.. | |
Protein Sequence | MSYKSAIIGLCLLAVILLAPPLAWHSHTKNIPAIILITWLLTMNLTCIVDAAIWSDDDFLTRWDGKGWCDIVIKLQVGANIGISCAVTNIIYNLHTILKADSVLPDLSSWTKIVKDLVISLFTPVMVMGFSYLLQVFRYGIARYNGCQNLLSPTWITTVLYTMWMLIWSFVGAVYATLVLFVFYKKRKDVRDILHCTNSGLNLTRFARLLIFCFIIILVMFPFSVYTFVQDLQQVEGHYTFKNTHSSTIWNTIIKFDPGRPIYNIWLYVLMSYLVFLIFGLGSDALHMYSKFLRSIKLGFVLDMWKRFIDKNKEKRVGILLNKLSSRKESRNPFSTDSENYISTCTENYSPCVGTPISQAHFYVDYRIPDDPRKSQNKSKKYLFADKETDDILDEIDLKESRHIPYVTQGQSFDDEISLGGFSKVTLDYSEKLHNSASSNFEGESLCYSPASKEENSSSNEHSSENTAGP | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
108 | Phosphorylation | DSVLPDLSSWTKIVK CCCCCCHHHHHHHHH | 31.07 | 21440633 | |
111 | Phosphorylation | LPDLSSWTKIVKDLV CCCHHHHHHHHHHHH | 16.91 | 21440633 | |
323 | Acetylation | RVGILLNKLSSRKES HHHHHHHHHHCCCHH | 50.11 | 24489116 | |
323 | Ubiquitination | RVGILLNKLSSRKES HHHHHHHHHHCCCHH | 50.11 | 24961812 | |
375 | Phosphorylation | IPDDPRKSQNKSKKY CCCCCCCCCCCCCCE | 40.02 | 25005228 | |
387 | Ubiquitination | KKYLFADKETDDILD CCEEECCCCCCCCHH | 60.11 | 24961812 | |
399 | Ubiquitination | ILDEIDLKESRHIPY CHHHCCCCHHCCCCE | 50.31 | 24961812 | |
408 | Phosphorylation | SRHIPYVTQGQSFDD HCCCCEECCCCCCCC | 22.57 | 30377154 | |
412 | Phosphorylation | PYVTQGQSFDDEISL CEECCCCCCCCCCCC | 37.15 | 21440633 | |
418 | Phosphorylation | QSFDDEISLGGFSKV CCCCCCCCCCCCEEE | 20.93 | 21440633 | |
424 | Ubiquitination | ISLGGFSKVTLDYSE CCCCCCEEEEEECHH | 36.66 | - | |
426 | Phosphorylation | LGGFSKVTLDYSEKL CCCCEEEEEECHHHH | 20.04 | 21440633 | |
430 | Phosphorylation | SKVTLDYSEKLHNSA EEEEEECHHHHHCCC | 28.11 | 25521595 | |
432 | Ubiquitination | VTLDYSEKLHNSASS EEEECHHHHHCCCCC | 49.45 | - | |
436 | Phosphorylation | YSEKLHNSASSNFEG CHHHHHCCCCCCCCC | 20.84 | 20377248 | |
438 | Phosphorylation | EKLHNSASSNFEGES HHHHCCCCCCCCCCC | 26.15 | 20377248 | |
439 | Phosphorylation | KLHNSASSNFEGESL HHHCCCCCCCCCCCC | 45.30 | 20377248 | |
445 | Phosphorylation | SSNFEGESLCYSPAS CCCCCCCCCCCCCCC | 34.30 | 20377248 | |
449 | Phosphorylation | EGESLCYSPASKEEN CCCCCCCCCCCCCCC | 17.00 | 21551504 | |
452 | Phosphorylation | SLCYSPASKEENSSS CCCCCCCCCCCCCCC | 43.94 | 20377248 | |
453 | Ubiquitination | LCYSPASKEENSSSN CCCCCCCCCCCCCCC | 71.76 | - | |
458 | Phosphorylation | ASKEENSSSNEHSSE CCCCCCCCCCCCCCC | 49.08 | 21551504 | |
464 | Phosphorylation | SSSNEHSSENTAGP- CCCCCCCCCCCCCC- | 36.45 | 28889911 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of STE3_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of STE3_YEAST !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of STE3_YEAST !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
AKR1_YEAST | AKR1 | physical | 9243510 | |
GBB_YEAST | STE4 | genetic | 2104659 | |
RCC1_YEAST | SRM1 | genetic | 2548085 | |
ASG7_YEAST | ASG7 | genetic | 11073982 | |
STE20_YEAST | STE20 | genetic | 8754848 | |
PEX15_YEAST | PEX15 | physical | 16093310 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-430, AND MASSSPECTROMETRY. |